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Literature summary for 3.2.1.14 extracted from

  • Ishisaki, K.; Honda, Y.; Taniguchi, H.; Hatano, N.; Hamada, T.
    Heterogonous expression and characterization of a plant class IV chitinase from the pitcher of the carnivorous plant Nepenthes alata (2011), Glycobiology, 22, 345-351.
    View publication on PubMed
Search for more literature for 3.2.1.14

Cloned(Commentary)

Cloned (Comment) Organism
recombinant expression in Escherichia coli strain BL21 (DE3) as His6-Nus-His6-NaCHIT1 fusion protein. The fusion protein is cleaved by HRV 3C protease resulting in a soluble and active NaCHIT1 Nepenthes alata

Localization

Localization Comment Organism GeneOntology No. Textmining
extracellular
-
 Nepenthes alata
-
-

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
29000
-
 x * 29000, recombinant soluble NaCHIT1, SDS-PAGE Nepenthes alata

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Nepenthes alata the enzyme exhibits weak activity toward polymeric substrates and significant activity toward (GlcNAc)n (n=4-6). The anomeric form of the products indicate an inverting enzyme ?
-
 ?

Organism

Organism UniProt Comment Textmining
Nepenthes alata
-
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant His6-Nus-His6-NaCHIT1 fusion protein from Escherichia coli strain BL21 (DE3) by metal affinity chromatography Nepenthes alata

Source Tissue

Source Tissue Comment Organism Textmining
pitcher secretion
-
 Nepenthes alata
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information the enzyme exhibits weak activity toward polymeric substrates and significant activity toward (GlcNAc)n (n=4-6). The anomeric form of the products indicate an inverting enzyme Nepenthes alata ?
-
 ?
additional information no activity with N,N',N''-triacetylchitotriose Nepenthes alata ?
-
 ?
N,N',N'',N''', N'''',N'''''-hexaacetylchitohexaose + H2O the enzyme hydrolyzes the third and fourth glycosidic linkages from the non-reducing end of N,N',N'',N''', N'''',N'''''-hexaacetylchitohexaose Nepenthes alata N-acetyl-D-glucosamine + N,N'-diacetylchitobiose + N,N',N''-triacetylchitotriose + N,N',N'',N'''-tetraacetylchitotetraose
-
 ?
N,N',N'',N''',N''''-pentaacetylchitopentaose + H2O the enzyme hydrolyzed N,N',N'',N''',N''''-pentaacetylchitopentaose at the third linkage from the non-reducing end Nepenthes alata N,N'-diacetylchitobiose + N,N',N''-triacetylchitotriose
-
 ?
N,N',N'',N'''-tetraacetylchitotetraose + H2O
-
 Nepenthes alata N-acetyl-D-glucosamine + N,N'-diacetylchitobiose + N,N',N''-triacetylchitotriose
-
 ?

Subunits

Subunits Comment Organism
? x * 29000, recombinant soluble NaCHIT1, SDS-PAGE Nepenthes alata

Synonyms

Synonyms Comment Organism
class IV chitinase
-
 Nepenthes alata
More the enzyme belongs to the GH19 family Nepenthes alata
NaCHIT1
-
 Nepenthes alata

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
60
-
-
 Nepenthes alata

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
5.5
-
-
 Nepenthes alata

General Information

General Information Comment Organism
additional information deletion of four loops likely leads the enzyme to optimize the (beta-1,4-GlcNAc)n hydrolytic reaction rather than hydrolysis of polymeric substrates Nepenthes alata
physiological function chitinase hydrolyzes the beta-1,4 glycosidic bond of chitin, the linear polysaccharide of GlcNAc, to produce chitooligosaccharides Nepenthes alata

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
additional information
-
 additional information the kcat/Km of the (beta-1,4-GlcNAc)n hydrolysis increases with an increase in the degree of polymerization of the substrates Nepenthes alata